Results 151 to 160 of about 45,459 (207)

Parvalbumin immunoreactivity in the rat retina

Neuroscience Letters, 1990
The distribution of the Ca2+ binding protein parvalbumin was studied in the rat retina with immunocytochemistry using a mouse monoclonal antibody. Specific parvalbumin immunoreactivity was identified within a subpopulation of ganglion cells and a subpopulation of amacrine cells.
Pietro Paolo Sanna, F E Bloom
exaly   +3 more sources

Parvalbumin in Human Brain

Journal of Neurochemistry, 1985
Abstract: Parvalbumin was isolated from human cerebral cortex and biceps and triceps muscles by HPLC. The immunological properties of the human protein and the mobility in two‐dimensional polyacrylamide gels were similar to that of parvalbumin isolated from the muscles of rat, mouse, rabbit, and chicken.
M W, Berchtold, M R, Celio, C W, Heizmann   +2 more
openaire   +2 more sources

Parvalbumin as a Pleomorphic Protein

Current Protein & Peptide Science, 2017
Parvalbumin (PA) is a classical small, mostly cytosolic Ca2+-binding protein of the EF-hand superfamily expressed in vertebrates in a tissue- and cell-specific manner, serving as a magnesium/ calcium buffer. In the last decade novel data were published on structural peculiarities of PA, likely affecting its functionality.
Permyakov, Eugene, Uversky, Vladimir, Permyakov, Sergei   +2 more
openaire   +3 more sources

Binding of nucleotides to parvalbumins

Biochemical and Biophysical Research Communications, 1982
Abstract Intrinsic fluorescence and equilibrium dialysis studies have shown that ATP and ADP bind to parvalbumin molecules with affinities allowing the complex formation at physiological concentrations of protein and nucleotides. The stoichiometry and association constants for the nucleotide binding to calcium-loaded, magnesium-loaded and metal free ...
E A, Permyakov, L P, Kalinichenko, V V, Yarmolenko, E A, Burstein, C, Gerday   +4 more
openaire   +2 more sources

Structure and Function of Parvalbumin

1989
Parvalbumins were first isolated from muscles of lower vertebrates and their primary structures and biochemical properties have been investigated intensively (for review see 1). Later, parvalbumins were also detected in skeletal muscles of higher vertebrates, and the rabbit and rat parvalbumin have been sequenced (for reviews see 2–4).
Heizmann CW, Kagi U
openaire   +3 more sources

Conformational studies on muscular parvalbumins cooperative binding of calcium (II) to parvalbumins

Biochimie, 1979
1H NMR and ORD were used to characterize the respective variations of tertiary structure and secondary structure of parvalbumins with calcium content ((Pa(O), without calcium and PaCa2 calcium saturated) and temperature. It has been observed that the tertiary structure can be lost without significant variation of the helical content.
A, Cave, M, Pages, P, Morin, C M, Dobson
openaire   +2 more sources

[Ca-inhibited binding of melittin with parvalbumin. A new role for parvalbumins?].

Molekuliarnaia biologiia, 1989
It was found that pike parvalbumins pI 4.2 and 5.0 bind amphiphilic peptide melittin extracted from bee venom in an extraordinary Ca-dependent manner: in apo-state the protein forms a tight equimolar complex with melittin (Ka = 10(6) M-1 at 18 degrees C); in Ca- (and Mg-) loaded state it does not take place.
E A, Permiakov, V N, Medvedkin, G A, Koreneĭchuk, E G, Kostrzhevskaia, A G, Murzin   +4 more
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Parvalbumin Isoforms in Zebrafish

Molecular Biology Reports, 2005
By using an analysis of existing genomic information it is concluded that in zebrafish nine genes encode parvalbumin (PV). These genes possess introns that differ in size and show nucleotide variability but they contain the same number of exons, and for each corresponding exon, the number of nucleotides therein are identical in all the paralogs.
openaire   +2 more sources